ID H3CJ21_TETNG Unreviewed; 913 AA.
AC H3CJ21;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=dolichyl-phosphate-mannose--protein mannosyltransferase {ECO:0000256|ARBA:ARBA00012839};
DE EC=2.4.1.109 {ECO:0000256|ARBA:ARBA00012839};
GN Name=TMTC1 {ECO:0000313|Ensembl:ENSTNIP00000008250.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000008250.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000008250.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the TMTC family.
CC {ECO:0000256|ARBA:ARBA00007882}.
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DR AlphaFoldDB; H3CJ21; -.
DR STRING; 99883.ENSTNIP00000008250; -.
DR Ensembl; ENSTNIT00000008416.1; ENSTNIP00000008250.1; ENSTNIG00000005551.1.
DR GeneTree; ENSGT00940000158027; -.
DR HOGENOM; CLU_011615_1_1_1; -.
DR InParanoid; H3CJ21; -.
DR OMA; TRWHTWR; -.
DR TreeFam; TF328339; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR013618; TMTC_DUF1736.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR44809; -; 1.
DR PANTHER; PTHR44809:SF1; PROTEIN O-MANNOSYL-TRANSFERASE TMTC1; 1.
DR Pfam; PF08409; TMTC_DUF1736; 1.
DR Pfam; PF13374; TPR_10; 2.
DR Pfam; PF13414; TPR_11; 1.
DR Pfam; PF13424; TPR_12; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13431; TPR_17; 1.
DR SMART; SM00386; HAT; 5.
DR SMART; SM00028; TPR; 10.
DR SUPFAM; SSF48439; Protein prenylyltransferase; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..913
FT /note="dolichyl-phosphate-mannose--protein
FT mannosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003582158"
FT TRANSMEM 88..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..487
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 323..395
FT /note="DUF1736"
FT /evidence="ECO:0000259|Pfam:PF08409"
FT REPEAT 514..547
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 579..612
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 613..646
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 647..680
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 714..747
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 782..815
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 820..853
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 854..887
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 227..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 102437 MW; F7CA1607DB60D061 CRC64;
GTYRAGRYVV LASLCVLCYG NSVHGELVHD DVWAIVNNPD VRADSSLRKI FSNDFWKPMS
DNTSHKSYRP LCILTFKLNI LLHGMSPFYF HITNLLLHCA VTCLLMYTCE CCVFEDGHLA
FVTALIFAVH PIHTEAVAGV VGRADVLACM LFLLAFLSYI RSVGVCLTED VLPPTVSVGC
LVISVLLGTC AMLVKETGIT VFGVCIIYDA LVLCRKPLGQ QNAAISSPET VKKGKGKPKQ
VGSSRREGML EMSKDEDENC GCSGRGQGVS LEDRANWNIL LRHMSGSRFR DLLHVSGPFT
KRAGFISVCV IIVLSVRLWL MGGSMPLFSE QDNPASFSPY LLTRILTYSY LLSFNAWLLL
VPAVLCYDWQ VGSIPLVESL ADLRNGATVL LALVILTLCV RCIFALQNLE SREILVGVLF
LVFPFIPASN LFFRVGFVVA ERVLYMPSMG YCILVALGVG RLCTVVGRYG ATVVSVSVVL
LLLFFSWKTV HQNQVWLSRE ALFRSGIQTL PHNAKVHYNY ANFLKDSGQL QEAIRHYSTA
LRLYPQHASA MNNLGTLTQS PEEAESYYRK ALAINPQHNR ALFNLGNLFK SQGKEKEAES
LLKDSIHFGP HFANAYSSLA SLYAEQKRFF EAKEVYLKGI EKCPENSDLH NNYGVFLVDT
GEDERAVDHY QQAIRLKPTH YIAMVNLGRL LRLNNKNQEA EFWYKRALRV TKKADILTPL
GALYYNTGRY EEALQVYREA TSLQPDNTDI WLAFAQVLAV ADRSGEAEKL TLEIISKEIS
CVECYRLLSA IYSKRGNYTE ALGALDRALQ QNLTDVTVRA ELYFSKGNQL REMNLLEQAF
KSYELAVELK PDQSQAWMNM GGIRHMKGDY AAARMYYQRA LLLNPGSKLL KENLAKLDRL
ERRLSALRRP DQT
//
